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The acceleration effect of chondroitin-4-sulfate(CS) proteoglycan on the processing of procathepsin L in vitro was investigated using enzyme purified from the culture medium of MLC cells. Procathepsin L was slightly processed even when it was incubated without CSproteoglycan for 60 min in 50 mM acetate buffer, pH 5.5, and trace amounts of the 31 kDa mature form and 35  38 kDa intermediates of cathepsin L were formed. On the other hand, in the presence of CSproteoglycan, procathepsin L was completely converted to the mature form within the same 60 minute time period. Moreover, ZPheArgMCA hydrolyzing activity was increased significantly by the incubation with CSproteoglycan, while no considerable increase in the activity was observed during the incubation without CSproteoglycan. Since the specific cathepsin L inhibitor, CLIK-195, inhibited the processing of procathepsin L accelerated by CSproteoglycan, the trace amount of cathepsin L activity may participate in the processing. These results suggest that CSproteoglycan may play a role in accelerating the processing of procathepsin L as an endogenous enhancer in the extracellular environment in vivo.

Chondroitin Sulfate Proteoglycan Is a Potent Enhancer in the Processing of Procathepsin L